Saturable triiodothyronine-binding sites in the pituitary nuclei of salmonid teleost fish.
High-affinity, limited-capacity, 3,5,3'-triiodo-L-thyronine (T3)-binding sites were established by in vitro saturation analysis in cell nuclei of the pituitary gland of arctic charr. The sites were extracted from the purified nuclei using 0.4 M NaCl and incubated with [125I]T3 in the presence of 0.2 M NaCl. T3 saturable binding attained equilibrium after 18-24 hr of incubation at 4 degrees. The association constant ranged from 6.7 to 20.1 liters.mol-1 x 10(9), indicating a T3 affinity greater than that for T3-binding sites in rainbow trout liver. The maximal binding capacity ranged from 0.93 to 2.05 10(-13) mol.mg DNA-1, representing a mean site abundance corresponding to 60% of that for nuclei from trout liver. Thyroxine (T4) completely displaced [125I]T3 in the pituitary nuclei of arctic charr and T3 completely displaced [125I]T4 in the pituitary nuclei of rainbow trout, suggesting that in salmonids both T4 and T3 bind to the same single class of sites. However, the site affinity for T4 was approximately 20-50x less than that for T3. The possible roles of these sites in pituitary function as well as their relationship to other nuclear T3-binding sites in salmonid fish are discussed.
Bres
O
O
Department of Zoology, University of Manitoba, Winnipeg, Canada.
Eales
J G
JG
D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism*; D004247:DNA / Q000378:metabolism; D006801:Humans; D007457:Iodine Radioisotopes; D007700:Kinetics; D009687:Nuclear Proteins / Q000378:metabolism; D010902:Pituitary Gland / Q000166:cytology / Q000378:metabolism* / Q000648:ultrastructure; D011988:Receptors, Thyroid Hormone / Q000032:analysis / Q000378:metabolism*; D012487:Salmonidae / Q000378:metabolism*; D014337:Trout / Q000378:metabolism*
D007457:Iodine Radioisotopes; D009687:Nuclear Proteins; D011988:Receptors, Thyroid Hormone; D004247:DNA